(Q32064358)

6 July 2017

title

A six-module human nebulin fragment bundles actin filaments and induces actin polymerization (English)

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6 July 2017

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Gonsior SM

1

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6 July 2017

Gautel M

series ordinal

2

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6 July 2017

Hinssen H

series ordinal

3

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6 July 2017

publication date

1 April 1998

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Journal of Muscle Research & Cell Motility

6 July 2017

published in

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6 July 2017

volume

19

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6 July 2017

issue

3

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6 July 2017

page(s)

225-235

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Nebulin, a helical actin binding protein

6 July 2017

cites work

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12 December 2020

Molecular contacts between nebulin and actin: cross-linking of nebulin modules to the N-terminus of actin

1 reference

12 December 2020

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

12 December 2020

Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin

1 reference

12 December 2020

Nebulette: a 107 kD nebulin-like protein in cardiac muscle

1 reference

12 December 2020

Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation

1 reference

12 December 2020

Purification and Characterization of Nebulin Subfragments Produced by 0.1 mM CaCl21

1 reference

12 December 2020

Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line

1 reference

12 December 2020

Nebulin as an actin zipper. A two-module nebulin fragment promotes actin nucleation and stabilizes actin filaments.

1 reference

12 December 2020

The organization of titin (connectin) and nebulin in the sarcomeres: an immunocytolocalization study

1 reference

12 December 2020

Myogenesis in the mouse embryo: differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly

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12 December 2020

Evidence from electron microscope studies on actin paracrystals concerning the origin of the cross-striation in the thin filaments of vertebrate skeletal muscle.

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12 December 2020

Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors

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12 December 2020

The complete primary structure of human nebulin and its correlation to muscle structure

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12 December 2020

Cloning, expression, and protein interaction of human nebulin fragments composed of varying numbers of sequence modules

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12 December 2020

Effect of capping protein on the kinetics of actin polymerization.

1 reference

12 December 2020

Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3.

1 reference

12 December 2020

Fluorescence microscopy: reduced photobleaching of rhodamine and fluorescein protein conjugates by n-propyl gallate

1 reference

12 December 2020

Behaviour of connectin (titin) and nebulin in skinned muscle fibres released after extreme stretch as revealed by immunoelectron microscopy

1 reference

12 December 2020

The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin

1 reference

12 December 2020

Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin

1 reference

12 December 2020

Correlation Between Conformational and Binding Properties of Nebulin Repeats

1 reference

12 December 2020

Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile

1 reference

12 December 2020

Towards a molecular understanding of titin

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12 December 2020

Phalloidin unzips nebulin from thin filaments in skeletal myofibrils

1 reference

12 December 2020

Evidence that nebulin is a protein-ruler in muscle thin filaments

1 reference

12 December 2020

Identifiers

DOI

10.1023/A:1005372915268

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Dimensions Publication ID

6 July 2017

1019335810

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